Post Doc/Research Associate Position to Study Role of Glycosylation
in Reproduction, Development, and Inflammation.
Glycobiology is a rapidly growing field with an impact in many
areas involving folding and assembly of newly synthesized
glycoproteins, control of circulatory half life, targeting to
tissues and organelles, and cellular recognition during inflammation
and development. My laboratory studies unique carbohydrate
structures which serve a recognition function, glycosyltransferases
which synthesize them, and how their recognition determinants
interact with specific receptors. For example, we have found that
structures containing GalNAc-4-SO4 are present on the pituitary
glycoprotein hormones LH and TSH, playing a critical role in hormone
activity via hormone clearance by a GalNAc-4-SO4-specific receptor
in liver endothelial cells. Using biochemical and molecular
biologic approaches, we examine how glycosyltransferases recognize
their target proteins to synthesize these structures, and how
glycosyltransferase and receptor expression are regulated during
development and hormonal cycles. We are also examining the roles
played by these structures in recognition during inflammation and
development. We have recently cloned two of these transferases and
are embarking on studies directed at understanding regulation of
expression, structural-function relationships, and biologic function
Interested candidates with experience in molecular biology and/or
protein purification and characterization should contact: Dr.
Jacques U. Baenziger, Department of Pathology, Washington University
Medical School, St. Louis, MO 63110 with a CV and references.
FAX 314-362-8888. E-mail <Baenziger at Pathology.WUSTL.EDU>
Hooper, L.V., Hindsgaul, O., and Baenziger, J.U.: Purification and
characterization of the GalNAc-4-sulfotransferase responsible for
sulfation of GalNAcb1,4-GlcNAc-bearing oligosaccharides. J. Biol.
Chem. 270:16327-16332, 1995.
Manzella, S.M., Beranek, M.C., Dharmesh, S.M., Swanson, P., and
Baenziger, J.U.: Evolutionary conservation of sulfated
oligosaccharides on vertebrate glycoprotein hormones that control
circulatory half-life. J. Biol. Chem. 270:21665-21671, 1995.
Mengeling, B.J., Manzella, S.M., and Baenziger, J.U.: A cluster of
basic amino acids within an a-helix is essential for a-subunit
recognition by the glycoprotein hormone:
N-acetylgalactosaminyltransferase. Proc. Natl. Acad. Sci. USA
Baenziger, J.U.: Protein-specific glycosyltransferases: How and
why they do it! FASEB J. 8:1019-1025, 1994.
Dharmesh, S.M. and Baenziger, J.U.: Estrogen modulates expression
of the glycosyltransferases which synthesize sulfated
oligosaccharides on lutropin. Proc. Natl. Acad. Sci. USA
Baenziger, J.U., Kumar, S., Brodbeck, R.M., Smith, P.L. and Beranek,
M.C.: Circulatory half-life but not interaction with the LH/CG
receptor is modulated by sulfation of bLH oligosaccharides. Proc.
Natl. Acad. Sci. USA 89:334-338, 1992.
Fiete, D., Srivastava, V., Hindsgaul, O. and Baenziger, J.U.: A
hepatic reticulo-endothelial cell receptor specific for
S04-4GalNAcb1,4GlcNAcb1,2Mana that mediates rapid clearance of
lutropin. Cell, 67:1103-1110, 1991.